Purification and properties of dicarboxylate ω-amidase from Bacillus subtilis 168 and Thermus aquaticus YT-1
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference26 articles.
1. Identification of the predominant protein phosphorylated by ATP in extracts of Bacillus subtilis as nucleoside diphosphokinase
2. Dicarboxylate ω-amidase of Bacillus subtilis-168: Evidence for a membrane-associated form
3. HYDROLYSIS AND TRANSFER REACTIONS CATALYZED BY ω-AMIDASE PREPARATIONS
4. Rat liver ι-amidase. Purification and properties
5. 5-Hydroxy-N-methylpyroglutamate Synthetase
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1. Molecular identification of ω-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2;Biochimie;2009-09
2. Assay and purification of ω-amidase/Nit2, a ubiquitously expressed putative tumor suppressor, that catalyzes the deamidation of the α-keto acid analogues of glutamine and asparagine;Analytical Biochemistry;2009-08
3. A Novel Amidase (Half-Amidase) for Half-Amide Hydrolysis Involved in the Bacterial Metabolism of Cyclic Imides;Applied and Environmental Microbiology;2000-05
4. Novel malonamidases in Bradyrhizobium japonicum. Purification, characterization, and immunological comparison.;Journal of Biological Chemistry;1994-03
5. Omega-amidase;Enzyme Handbook 4;1991
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